Gates and Latches: the mechanochemistry of ATP binding in kinesin 1 and Eg5

This thesis explores the role of mechanochemistry in two biological systems. The first system investigated involves cargo transport along microtubule filaments by Kinesin 1. A gating mechanism is needed to coordinate ATP binding to the two catalytic domains within Kinesin 1 in order to prevent simultaneous binding, hydrolysis and detachment of both heads which could prematurely terminate cargo transport. The second system investigated involves cell division and the mitotic kinesin Eg5. In this motor, we investigate ATP-binding and find that it has an additional component internal to its catalytic domain, called Loop 5, which is functionally important for both ATP binding and neck linker docking.

Author dc:creator

• Behnke-Parks, William M.

• Biology
• Biophysics
• Biochemistry
• Kinesin
• Mechanical chemistry
• Cell division

Language dc:language

English

DOI dc:identifier

https://doi.org/10.7916/D83B66HW

OAI identifier oai:identifier

oai:academiccommons.columbia.edu:10.7916/D83B66HW